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P28298

- ACEA_EMENI

UniProt

P28298 - ACEA_EMENI

Protein

Isocitrate lyase

Gene

acuD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Isocitrate = succinate + glyoxylate.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei206 – 2061

    GO - Molecular functioni

    1. isocitrate lyase activity Source: ASPGD
    2. methylisocitrate lyase activity Source: ASPGD

    GO - Biological processi

    1. acetate catabolic process Source: ASPGD
    2. carbon utilization Source: ASPGD
    3. fatty acid catabolic process Source: ASPGD
    4. glyoxylate cycle Source: UniProtKB-UniPathway
    5. propionate catabolic process, 2-methylcitrate cycle Source: ASPGD
    6. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00703; UER00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate lyase (EC:4.1.3.1)
    Short name:
    ICL
    Short name:
    Isocitrase
    Short name:
    Isocitratase
    Gene namesi
    Name:acuD
    ORF Names:AN5634
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome V

    Subcellular locationi

    GO - Cellular componenti

    1. glyoxysome Source: UniProtKB-SubCell
    2. peroxisomal matrix Source: ASPGD
    3. peroxisome Source: ASPGD

    Keywords - Cellular componenti

    Glyoxysome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 538538Isocitrate lyasePRO_0000068790Add
    BLAST

    Expressioni

    Inductioni

    By acetate.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00003436.

    Structurei

    Secondary structure

    1
    538
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi18 – 225
    Helixi25 – 295
    Helixi36 – 427
    Helixi52 – 6918
    Beta strandi73 – 775
    Helixi81 – 9010
    Beta strandi94 – 963
    Helixi98 – 1047
    Helixi122 – 14625
    Helixi150 – 1534
    Beta strandi165 – 1684
    Beta strandi173 – 1753
    Helixi176 – 18813
    Beta strandi192 – 1965
    Beta strandi212 – 2143
    Helixi217 – 23317
    Beta strandi239 – 2435
    Helixi246 – 2483
    Beta strandi249 – 2535
    Helixi258 – 2636
    Beta strandi264 – 2674
    Helixi275 – 28410
    Helixi290 – 30213
    Helixi309 – 3179
    Helixi324 – 33512
    Helixi340 – 35112
    Beta strandi369 – 3713
    Helixi375 – 38511
    Beta strandi390 – 3934
    Helixi401 – 41212
    Beta strandi419 – 4235
    Beta strandi426 – 4283
    Helixi430 – 4323
    Helixi436 – 4405
    Helixi442 – 4487
    Beta strandi451 – 4566
    Helixi459 – 47820
    Helixi480 – 4867
    Helixi488 – 4947
    Helixi497 – 4993
    Helixi501 – 5055
    Helixi507 – 51812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DQUX-ray2.80A1-538[»]
    ProteinModelPortaliP28298.
    SMRiP28298. Positions 2-520.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28298.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2224.
    HOGENOMiHOG000238475.
    KOiK01637.
    OMAiALISHQF.
    OrthoDBiEOG73Z331.

    Family and domain databases

    Gene3Di3.20.20.60. 2 hits.
    InterProiIPR006254. Isocitrate_lyase.
    IPR018523. Isocitrate_lyase_ph_CS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
    PfamiPF00463. ICL. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR01346. isocit_lyase. 1 hit.
    PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28298-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYIEEEDQR YWDEVAAVKN WWKDSRWRYT KRPFTAEQIV AKRGNLKIEY    50
    PSNVQAKKLW GILERNFKNK EASFTYGCLD PTMVTQMAKY LDTVYVSGWQ 100
    SSSTASSTDE PSPDLADYPM NTVPNKVNHL WMAQLFHDRK QREERMTTPK 150
    DQRHKVANVD YLRPIIADAD TGHGGLTAVM KLTKLFVERG AAGIHIEDQA 200
    PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA IARTDSEAAT 250
    LITSTIDHRD HPFIIGSTNP DIQPLNDLMV MAEQAGKNGA ELQAIEDEWL 300
    AKAGLKLFND AVVDAINNSP LPNKKAAIEK YLTQSKGKSN LEARAIAKEI 350
    AGTDIYFDWE APRTREGYYR YQGGTQCAIN RAVAYAPFAD LIWMESKLPD 400
    YKQAKEFADG VHAVWPEQKL AYNLSPSFNW KKAMPRDEQE TYIKRLGALG 450
    YAWQFITLAG LHTTALISDT FAKAYAKQGM RAYGELVQEP EMANGVDVVT 500
    HQKWSGANYV DNMLKMITGG VSSTAAMGKG VTEDQFKS 538
    Length:538
    Mass (Da):60,321
    Last modified:May 1, 2007 - v3
    Checksum:i21B5B56E5345681E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171Missing in CAA44572. (PubMed:1531185)Curated
    Sequence conflicti68 – 681Missing in CAA44572. (PubMed:1531185)Curated
    Sequence conflicti157 – 1571A → T in CAA44572. (PubMed:1531185)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62696 Genomic DNA. Translation: CAA44572.1.
    AACD01000098 Genomic DNA. Translation: EAA62727.1.
    BN001305 Genomic DNA. Translation: CBF81510.1.
    PIRiS26857.
    RefSeqiXP_663238.1. XM_658146.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00003436; CADANIAP00003436; CADANIAG00003436.
    GeneIDi2871925.
    KEGGiani:AN5634.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62696 Genomic DNA. Translation: CAA44572.1 .
    AACD01000098 Genomic DNA. Translation: EAA62727.1 .
    BN001305 Genomic DNA. Translation: CBF81510.1 .
    PIRi S26857.
    RefSeqi XP_663238.1. XM_658146.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DQU X-ray 2.80 A 1-538 [» ]
    ProteinModelPortali P28298.
    SMRi P28298. Positions 2-520.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00003436.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00003436 ; CADANIAP00003436 ; CADANIAG00003436 .
    GeneIDi 2871925.
    KEGGi ani:AN5634.2.

    Phylogenomic databases

    eggNOGi COG2224.
    HOGENOMi HOG000238475.
    KOi K01637.
    OMAi ALISHQF.
    OrthoDBi EOG73Z331.

    Enzyme and pathway databases

    UniPathwayi UPA00703 ; UER00719 .

    Miscellaneous databases

    EvolutionaryTracei P28298.

    Family and domain databases

    Gene3Di 3.20.20.60. 2 hits.
    InterProi IPR006254. Isocitrate_lyase.
    IPR018523. Isocitrate_lyase_ph_CS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    PANTHERi PTHR21631:SF3. PTHR21631:SF3. 1 hit.
    Pfami PF00463. ICL. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMi SSF51621. SSF51621. 1 hit.
    TIGRFAMsi TIGR01346. isocit_lyase. 1 hit.
    PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the glyoxysomal isocitrate lyase genes of Aspergillus nidulans (acuD) and Neurospora crassa (acu-3)."
      Gainey L.D.S., Connerton I.F., Lewis E.H., Turner G., Ballance D.J.
      Curr. Genet. 21:43-47(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: R153.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans."
      Britton K.L., Langridge S.J., Baker P.J., Weeradechapon K., Sedelnikova S.E., De Lucas J.R., Rice D.W., Turner G.
      Structure 8:349-362(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiACEA_EMENI
    AccessioniPrimary (citable) accession number: P28298
    Secondary accession number(s): C8VFW4, Q5B1E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3